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• W2040470885 abstract "Glycosylation is one of the most common posttranslational modifications to occur in protein biosynthesis, yet its effect on the thermodynamics and kinetics of proteins is poorly understood. A minimalist model based on the native protein topology, in which each amino acid and sugar ring was represented by a single bead, was used to study the effect of glycosylation on protein folding. We studied in silico the folding of 63 engineered SH3 domain variants that had been glycosylated with different numbers of conjugated polysaccharide chains at different sites on the protein's surface. Thermal stabilization of the protein by the polysaccharide chains was observed in proportion to the number of attached chains. Consistent with recent experimental data, the degree of thermal stabilization depended on the position of the glycosylation sites, but only very weakly on the size of the glycans. A thermodynamic analysis showed that the origin of the enhanced protein stabilization by glycosylation is destabilization of the unfolded state rather than stabilization of the folded state. The higher free energy of the unfolded state is enthalpic in origin because the bulky polysaccharide chains force the unfolded ensemble to adopt more extended conformations by prohibiting formation of a residual structure. The thermodynamic stabilization induced by glycosylation is coupled with kinetic stabilization. The effects introduced by the glycans on the biophysical properties of proteins are likely to be relevant to other protein polymeric conjugate systems that regularly occur in the cell as posttranslational modifications or for biotechnological purposes." @default.
• W2040470885 created "2016-06-24" @default.
• W2040470885 creator A5024388057 @default.
• W2040470885 creator A5054904960 @default.
• W2040470885 date "2008-06-17" @default.
• W2040470885 modified "2023-10-16" @default.
• W2040470885 title "Effect of glycosylation on protein folding: A close look at thermodynamic stabilization" @default.
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• W2040470885 doi "https://doi.org/10.1073/pnas.0801340105" @default.
• W2040470885 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2448824" @default.
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